EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.37 | T148A | site-directed mutagenesis, the active site Thr148 mutation modulates the enzyme's strict amino acid substrate specificity | Mus musculus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.37 | additional information | - |
additional information | pre-steady state and steady state kinetics, overview | Mus musculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.37 | succinyl-CoA + glycine | Mus musculus | - |
5-aminolevulinate + CoA + CO2 | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.37 | Mus musculus | P08680 | - |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.3.1.37 | succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 | the rate of 5-aminolevulinate release is controlled by a hysteretic kinetic mechanism initiated by conformational changes of the enzyme. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity. Catalytic mechanism, overview | Mus musculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.37 | additional information | analysis of unstable enzyme-catalyzed reaction intermediates and conformational changes using physiological and non-physiological substrates and promiscuous T148A enzyme variant, overview. Formation of the quinonoid intermediate upon reacting glycine with the enzyme. Significantly, in the absence of the succinyl-CoA substrate, the external aldimine predominates over the glycine quinonoid intermediate. When instead of glycine, L-serine is reacted with the enzyme, a lag phase is observed in the progress curve for the L-serine external aldimine formation, indicating a hysteretic behavior in enzyme ALAS. Hysteresis is not detected in the T148A-catalyzed L-serine external aldimine formation. The rate of 5-aminolevulinate release is also controlled by a hysteretic kinetic mechanism. The active site residue Thr148 modulates the enzyme's strict amino acid substrate specificity, positioning of the glycine external aldimine in the active site, overview | Mus musculus | ? | - |
? | |
2.3.1.37 | succinyl-CoA + glycine | - |
Mus musculus | 5-aminolevulinate + CoA + CO2 | - |
r | |
2.3.1.37 | succinyl-CoA + L-serine | the reaction with L-serine follows a biphasic kinetic process | Mus musculus | ? | - |
? | |
2.3.1.37 | succinyl-CoA + O-methylglycine | - |
Mus musculus | ? | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | 18 | - |
assay at | Mus musculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | 7.5 | - |
assay at | Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.37 | pyridoxal 5'-phosphate | dependent on | Mus musculus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.37 | metabolism | 5-aminolevulinate synthase catalyzs the initial step of mammalian heme biosynthesis | Mus musculus |